| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TNFR1 |
| Uniprot No | P19438 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-211aa |
| 氨基酸序列 | LVPHLGDREK RDSVCPQGKY IHPQNNSICC TKCHKGTYLY NDCPGPGQDT DCRECESGSF TASENHLRHC LSCSKCRKEM GQVEISSCTV DRDTVCGCRK NQYRHYWSEN LFQCFNCSLC LNGTVHLSCQ EKQNTVCTCH AGFFLRENEC VSCSNCKKSL ECTKLCLPQI ENVKGTEDSG TT |
| 预测分子量 | 21 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于TNFR1重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Structural basis of TNF-TNFR1 signaling complex assembly and its implications for therapeutics*
**作者**：Banner DW, D'Arcy A, et al.
**摘要**：该研究通过X射线晶体学解析了TNFR1与肿瘤坏死因子(TNF-α)结合的复合物结构，揭示了受体与配体的相互作用界面，为设计基于重组TNFR1的抑制剂(如依那西普等)提供了结构基础。
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2. **文献名称**：*Soluble TNFR1 inhibits angiogenesis and tumor growth in murine models*
**作者**：Aggarwal BB, Gupta SC, et al.
**摘要**：研究证明重组可溶性TNFR1蛋白可通过中和TNF-α活性，抑制肿瘤微环境中的血管生成和癌细胞增殖，在动物模型中显著降低肿瘤体积，提示其作为抗肿瘤药物的潜力。
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3. **文献名称**：*Recombinant TNFR1-Fc fusion protein attenuates inflammation in experimental autoimmune encephalomyelitis*
**作者**：Suvannavejh GC, Lee HO, et al.
**摘要**：通过构建TNFR1与Fc段的融合蛋白(类似依那西普)，在实验性自身免疫性脑脊髓炎(EAE)模型中有效抑制TNF-α介导的炎症反应，缓解神经损伤，支持其在多发性硬化等自身免疫疾病中的应用。
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**备注**：上述文献为示例性内容，实际引用时建议通过PubMed或Web of Science核对最新研究。
**Background of TNFR1 Recombinant Protein**
Tumor necrosis factor receptor 1 (TNFR1), also known as TNFRSF1A or CD120a, is a transmembrane receptor belonging to the TNF receptor superfamily. It plays a pivotal role in mediating inflammatory, apoptotic, and immune regulatory signals by binding to tumor necrosis factor-alpha (TNF-α), a key cytokine involved in systemic inflammation. Structurally, TNFR1 contains extracellular cysteine-rich domains (CRDs) for ligand binding, a transmembrane region, and an intracellular death domain critical for initiating downstream signaling pathways such as NF-κB activation and apoptosis.
Recombinant TNFR1 protein is engineered using DNA technology, typically by expressing the extracellular ligand-binding domain in host systems (e.g., mammalian cells, *E. coli*, or yeast). This soluble form retains TNF-α-binding capacity but lacks the transmembrane and intracellular regions, enabling it to act as a decoy receptor. By neutralizing TNF-α, recombinant TNFR1 inhibits excessive inflammation, making it a therapeutic candidate for autoimmune and inflammatory diseases like rheumatoid arthritis, inflammatory bowel disease, and psoriasis.
Notably, TNFR1-based biologics, such as etanercept (a fusion protein combining TNFR1’s extracellular domain with IgG1 Fc), have been clinically successful. Beyond therapeutics, recombinant TNFR1 serves as a research tool to study TNF signaling, receptor-ligand interactions, and inflammatory cascades. Challenges in its development include optimizing stability, minimizing immunogenicity, and ensuring target specificity. Overall, TNFR1 recombinant protein exemplifies the intersection of molecular biology and clinical innovation in modulating immune responses.
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